Yeast alpha-tubulin suppressor Ats1/Kti13 relates to the Elongator complex and interacts with Elongator partner protein Kti11
- PMID: 18466297
- DOI: 10.1111/j.1365-2958.2008.06273.x
Yeast alpha-tubulin suppressor Ats1/Kti13 relates to the Elongator complex and interacts with Elongator partner protein Kti11
Abstract
The alpha-tubulin suppressor 1 (ATS1) gene and the killer toxin-insensitive 13 (KTI13) locus from Saccharomyces cerevisiae are allelic. The Ats1/Kti13 gene product interacts with the cell polarity factor Nap1 and promotes growth inhibition of S. cerevisiae by zymocin, a tRNAse toxin complex from Kluyveromyces lactis. Kti13 removal causes zymocin resistance, a trait that is typical of defects in the Elongator complex. Here, we show that Kti13 co-purifies with the Elongator partner protein Kti11 and that the Kti11 interaction, not the Nap1 partnership, requires the C-terminus of Kti13. Moreover, Kti13 functionally relates to roles of the Elongator complex in tRNA wobble uridine modification, tRNA suppression of nonsense (SUP4) and missense (SOE1) mutations and tRNA restriction by zymocin. Also, inactivation of Kti13 or Elongator rescues the thermosensitive growth defect of secretory mutants (sec2-59(ts), sec12-4(ts)), suggesting that Kti13 and Elongator affect secretion processes that depend on the GTP exchange factors Sec2 and Sec12 respectively. Distinct from tandem deletions in KTI13 and Elongator genes, a kti13Delta kti11Delta double deletion induces synthetic sickness or lethality. In sum, our data suggest that Kti13 and Kti11 support Elongator functions and that they both share Elongator-independent role(s) that are important for cell viability.
Similar articles
-
A versatile partner of eukaryotic protein complexes that is involved in multiple biological processes: Kti11/Dph3.Mol Microbiol. 2008 Sep;69(5):1221-33. doi: 10.1111/j.1365-2958.2008.06350.x. Epub 2008 Jul 4. Mol Microbiol. 2008. PMID: 18627462
-
KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin.Mol Microbiol. 2002 May;44(3):865-75. doi: 10.1046/j.1365-2958.2002.02928.x. Mol Microbiol. 2002. PMID: 11994165
-
tRNA and protein methylase complexes mediate zymocin toxicity in yeast.Mol Microbiol. 2008 Sep;69(5):1266-77. doi: 10.1111/j.1365-2958.2008.06358.x. Epub 2008 Jul 24. Mol Microbiol. 2008. PMID: 18657261
-
Zymocin, a composite chitinase and tRNase killer toxin from yeast.Biochem Soc Trans. 2007 Dec;35(Pt 6):1533-7. doi: 10.1042/BST0351533. Biochem Soc Trans. 2007. PMID: 18031261 Review.
-
Structures and Activities of the Elongator Complex and Its Cofactors.Enzymes. 2017;41:117-149. doi: 10.1016/bs.enz.2017.03.001. Epub 2017 Apr 12. Enzymes. 2017. PMID: 28601220 Review.
Cited by
-
RNA modifications and cancer.RNA Biol. 2020 Nov;17(11):1560-1575. doi: 10.1080/15476286.2020.1722449. Epub 2020 Feb 7. RNA Biol. 2020. PMID: 31994439 Free PMC article. Review.
-
Loss of anticodon wobble uridine modifications affects tRNA(Lys) function and protein levels in Saccharomyces cerevisiae.PLoS One. 2015 Mar 6;10(3):e0119261. doi: 10.1371/journal.pone.0119261. eCollection 2015. PLoS One. 2015. PMID: 25747122 Free PMC article.
-
Low-Rank and Sparse Matrix Decomposition for Genetic Interaction Data.Biomed Res Int. 2015;2015:573956. doi: 10.1155/2015/573956. Epub 2015 Jul 26. Biomed Res Int. 2015. PMID: 26273633 Free PMC article.
-
tRNA anticodon loop modifications ensure protein homeostasis and cell morphogenesis in yeast.Nucleic Acids Res. 2016 Dec 15;44(22):10946-10959. doi: 10.1093/nar/gkw705. Epub 2016 Aug 5. Nucleic Acids Res. 2016. PMID: 27496282 Free PMC article.
-
Wobble uridine modifications-a reason to live, a reason to die?!RNA Biol. 2017 Sep 2;14(9):1209-1222. doi: 10.1080/15476286.2017.1295204. Epub 2017 Feb 23. RNA Biol. 2017. PMID: 28277930 Free PMC article. Review.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
